Abstract
Abstract Circular dichroic measurements in peptide aromatic and visible absorption regions have been combined with fluorescence and sedimentation data to characterize the effects of heme binding to apocytochrome b5 upon the secondary and tertiary structure and the environment of the aromatic amino acid residues. At pH 7.5 heme binding causes a slight tightening of the tertiary structure and may increase the amount of ordered secondary structure. The environment of the buried tryptophan residue, which lies outside of the heme crevice, is also apparently unaltered in the apoprotein. This stable form of the apoprotein appears to retain the essential features of the tertiary structure required for heme binding and contrasts markedly with unfolded peptide species produced during reversible denaturation by nonpolar solvents.
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